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Volumn 99, Issue 3, 1999, Pages 313-322

Chronic phospholamban-sarcoplasmic reticulum calcium atpase interaction is the critical calcium cycling defect in dilated cardiomyopathy

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); PHOSPHOLAMBAN;

EID: 0033615645     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)81662-1     Document Type: Article
Times cited : (440)

References (52)
  • 1
    • 0030933063 scopus 로고    scopus 로고
    • MLP-deficient mice exhibit a disruption of cardiac cytoarchitectural organization, dilated cardiomyopathy, and heart failure
    • Arber, S., Hunter, J.J., Ross, J., Jr., Hongo, M., Sansig, G., Borg, J., Perriard, J.C., Chien, K.R., and Caroni, P. (1997). MLP-deficient mice exhibit a disruption of cardiac cytoarchitectural organization, dilated cardiomyopathy, and heart failure. Cell 88, 393-403.
    • (1997) Cell , vol.88 , pp. 393-403
    • Arber, S.1    Hunter, J.J.2    Ross Jr., J.3    Hongo, M.4    Sansig, G.5    Borg, J.6    Perriard, J.C.7    Chien, K.R.8    Caroni, P.9
  • 2
    • 0033017374 scopus 로고    scopus 로고
    • Enteroviral protease 2A cleaves dystrophin: Evidence of cytoskeletal disruption in an acquired cardiomyopathy
    • Badorff, C., Lee, G.H., Lamphear, B.J., Maitone, M.E., Campbell, K.P., Rhoads, R.E., and Knowlton, K.U. (1999). Enteroviral protease 2A cleaves dystrophin: evidence of cytoskeletal disruption in an acquired cardiomyopathy. Nat. Med. 5, 320-326.
    • (1999) Nat. Med. , vol.5 , pp. 320-326
    • Badorff, C.1    Lee, G.H.2    Lamphear, B.J.3    Maitone, M.E.4    Campbell, K.P.5    Rhoads, R.E.6    Knowlton, K.U.7
  • 3
    • 0001229903 scopus 로고    scopus 로고
    • Alterations in calcium handling in cardiac hypertrophy and heart failure
    • Balke, C.W., and Shorofsky, S.R. (1998). Alterations in calcium handling in cardiac hypertrophy and heart failure. Cardiovasc. Res. 37, 290-299.
    • (1998) Cardiovasc. Res. , vol.37 , pp. 290-299
    • Balke, C.W.1    Shorofsky, S.R.2
  • 5
    • 0032701644 scopus 로고    scopus 로고
    • Complexity in simplicity: Monogenie disorders and complex cardiomyopathies
    • Chen, J., and Chien, K.R. (1999). Complexity in simplicity: monogenie disorders and complex cardiomyopathies. J. Clin. Invest. 103, 1483-1485.
    • (1999) J. Clin. Invest. , vol.103 , pp. 1483-1485
    • Chen, J.1    Chien, K.R.2
  • 6
    • 0033520388 scopus 로고    scopus 로고
    • Stress pathways and heart failure
    • Chien, K.R. (1999). Stress pathways and heart failure. Cell 98, 555-558.
    • (1999) Cell , vol.98 , pp. 555-558
    • Chien, K.R.1
  • 8
    • 0000501967 scopus 로고    scopus 로고
    • Molecular and cellular biology of cardiac hypertrophy and failure
    • K. Chien, ed. (Cambridge, MA: W.B. Saunders Co.)
    • Chien, K.R., Grace, A.A., and Hunter, J.J. (1999). Molecular and cellular biology of cardiac hypertrophy and failure. In Molecular Basis of Cardiovascular Disease. K. Chien, ed. (Cambridge, MA: W.B. Saunders Co.), pp. 211-250.
    • (1999) Molecular Basis of Cardiovascular Disease , pp. 211-250
    • Chien, K.R.1    Grace, A.A.2    Hunter, J.J.3
  • 9
    • 33646325581 scopus 로고    scopus 로고
    • High efficiency long term cardiac expression of foreign genes in living mouse embryos and neonates
    • in press
    • Christensen, G., Minamisawa, S., Gruber, P., Wang, Y., and Chien, K.R. (1999). High efficiency long term cardiac expression of foreign genes in living mouse embryos and neonates. Circulation, in press.
    • (1999) Circulation
    • Christensen, G.1    Minamisawa, S.2    Gruber, P.3    Wang, Y.4    Chien, K.R.5
  • 11
    • 0033588050 scopus 로고    scopus 로고
    • Disruption of the sarcoglycan-sarcospan complex in vascular smooth muscle: A novel mechanism for cardiomyopathy and muscular dystrophy
    • Coral-Vazquez, R., Cohn, R.D., Moore, S.A., Hill, J.A., Weiss, R.M., Davisson, R.L., Straub, V., Barresi, R., Bansal, D., Hrstka, R.F., et al. (1999). Disruption of the sarcoglycan-sarcospan complex in vascular smooth muscle: a novel mechanism for cardiomyopathy and muscular dystrophy. Cell 98, 465-474.
    • (1999) Cell , vol.98 , pp. 465-474
    • Coral-Vazquez, R.1    Cohn, R.D.2    Moore, S.A.3    Hill, J.A.4    Weiss, R.M.5    Davisson, R.L.6    Straub, V.7    Barresi, R.8    Bansal, D.9    Hrstka, R.F.10
  • 14
    • 0027234582 scopus 로고
    • Targeted developmental overexpression of calmodulin induces proliferative and hypertrophic growth of cardiomyocytes in transgenic mice
    • Gruver, C.L., DeMayo, F., Goldstein, M.A., and Means, A.R. (1993). Targeted developmental overexpression of calmodulin induces proliferative and hypertrophic growth of cardiomyocytes in transgenic mice. Endocrinology 133, 376-388.
    • (1993) Endocrinology , vol.133 , pp. 376-388
    • Gruver, C.L.1    Demayo, F.2    Goldstein, M.A.3    Means, A.R.4
  • 15
    • 0001078987 scopus 로고    scopus 로고
    • Alterations of calcium-regulatory proteins in heart failure
    • Hasenfuss, G. (1998). Alterations of calcium-regulatory proteins in heart failure. Cardiovasc. Res. 37, 279-289.
    • (1998) Cardiovasc. Res. , vol.37 , pp. 279-289
    • Hasenfuss, G.1
  • 16
    • 0033574574 scopus 로고    scopus 로고
    • Loss of a gp130 cardiac muscle cell survival pathway is a critical event in the onset of heart failure during biomechanical stress
    • Hirota, H., Chen, J., Betz, U.A., Rajewsky, K., Gu, Y., Ross, J., Jr., Muller, W., and Chien, K.R. (1999). Loss of a gp130 cardiac muscle cell survival pathway is a critical event in the onset of heart failure during biomechanical stress. Cell 97, 189-198.
    • (1999) Cell , vol.97 , pp. 189-198
    • Hirota, H.1    Chen, J.2    Betz, U.A.3    Rajewsky, K.4    Gu, Y.5    Ross Jr., J.6    Muller, W.7    Chien, K.R.8
  • 17
    • 0033592754 scopus 로고    scopus 로고
    • Signaling pathways for cardiac hypertrophy and failure
    • Hunter, J.J., and Chien, K.R. (1999). Signaling pathways for cardiac hypertrophy and failure. N. Engl. J. Med. 341, 1276-1283.
    • (1999) N. Engl. J. Med. , vol.341 , pp. 1276-1283
    • Hunter, J.J.1    Chien, K.R.2
  • 19
    • 0030989981 scopus 로고    scopus 로고
    • Phospholamban inhibitory function is activated by depolymerization
    • Kimura, Y., Kurzydlowski, K., Tada, M., and MacLennan, D.H. (1997). Phospholamban inhibitory function is activated by depolymerization. J. Biol. Chem. 272, 15061-15064.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15061-15064
    • Kimura, Y.1    Kurzydlowski, K.2    Tada, M.3    MacLennan, D.H.4
  • 21
    • 0029061324 scopus 로고
    • Cardiac function in mice overexpressing the beta-adrenergic receptor kinase or a beta ARK inhibitor
    • Koch, W.J., Rockman, H.A., Samama, P., Hamilton, R.A., Bond, R.A., Milano, C.A., and Lefkowitz, R.J. (1995). Cardiac function in mice overexpressing the beta-adrenergic receptor kinase or a beta ARK inhibitor. Science 268, 1350-1353.
    • (1995) Science , vol.268 , pp. 1350-1353
    • Koch, W.J.1    Rockman, H.A.2    Samama, P.3    Hamilton, R.A.4    Bond, R.A.5    Milano, C.A.6    Lefkowitz, R.J.7
  • 22
    • 0029830352 scopus 로고    scopus 로고
    • Phospholamban: A prominent regulator of myocardial contractility
    • Koss, K.L., and Kranias, E.G. (1996). Phospholamban: a prominent regulator of myocardial contractility. Circ. Res. 79, 1059-1063.
    • (1996) Circ. Res. , vol.79 , pp. 1059-1063
    • Koss, K.L.1    Kranias, E.G.2
  • 23
    • 0030997029 scopus 로고    scopus 로고
    • The relative phospholamban and SERCA2 ratio: A critical determinant of myocardial contractility
    • Koss, K.L., Grupp, I.L., and Kranias, E.G. (1997). The relative phospholamban and SERCA2 ratio: a critical determinant of myocardial contractility. Basic Res. Cardiol. 92, 17-24.
    • (1997) Basic Res. Cardiol. , vol.92 , pp. 17-24
    • Koss, K.L.1    Grupp, I.L.2    Kranias, E.G.3
  • 24
    • 0032054635 scopus 로고    scopus 로고
    • Calcium content of the sarcoplasmic reticulum in isolated ventricular myocytes from patients with terminal heart failure
    • Lindner, M., Erdmann, E., and Beuckelmann, D.J. (1998). Calcium content of the sarcoplasmic reticulum in isolated ventricular myocytes from patients with terminal heart failure. J. Mol. Cell. Cardiol. 30, 743-749.
    • (1998) J. Mol. Cell. Cardiol. , vol.30 , pp. 743-749
    • Lindner, M.1    Erdmann, E.2    Beuckelmann, D.J.3
  • 25
    • 0027932798 scopus 로고
    • Targeted ablation of the phospholamban gene is associated with markedly enhanced myocardial contractility and loss of beta-agonist stimulation
    • Luo, W., Grupp, I.L., Harrer, J., Ponniah, S., Grupp, G., Duffy, J.J., Doetschman, T., and Kranias, E.G. (1994). Targeted ablation of the phospholamban gene is associated with markedly enhanced myocardial contractility and loss of beta-agonist stimulation. Circ. Res. 75, 401-409.
    • (1994) Circ. Res. , vol.75 , pp. 401-409
    • Luo, W.1    Grupp, I.L.2    Harrer, J.3    Ponniah, S.4    Grupp, G.5    Duffy, J.J.6    Doetschman, T.7    Kranias, E.G.8
  • 26
    • 0032548847 scopus 로고    scopus 로고
    • Transgenic approaches to define the functional role of dual site phospholamban phosphorylation
    • Luo, W., Chu, G., Sato, Y., Zhou, Z., Kadambi, V.J., and Kranias, E.G. (1998). Transgenic approaches to define the functional role of dual site phospholamban phosphorylation. J. Biol. Chem. 273, 4734-4739.
    • (1998) J. Biol. Chem. , vol.273 , pp. 4734-4739
    • Luo, W.1    Chu, G.2    Sato, Y.3    Zhou, Z.4    Kadambi, V.J.5    Kranias, E.G.6
  • 27
    • 0033560011 scopus 로고    scopus 로고
    • Modification of postsynaptic densities after transient cerebral ischemia: A quantitative and three-dimensional ultrastructural study
    • Marione, M.E., Jones, Y.Z., Young, S.J., Ellisman, M.H., Zivin, J.A., and Hu, B.R. (1999). Modification of postsynaptic densities after transient cerebral ischemia: a quantitative and three-dimensional ultrastructural study. J. Neurosci. 19, 1988-1997.
    • (1999) J. Neurosci. , vol.19 , pp. 1988-1997
    • Marione, M.E.1    Jones, Y.Z.2    Young, S.J.3    Ellisman, M.H.4    Zivin, J.A.5    Hu, B.R.6
  • 28
    • 0030849445 scopus 로고    scopus 로고
    • Collaborative roles for c-Jun N-terminal kinase, c-Jun, serum response factor, and Sp1 in calcium-regulated myocardial gene expression
    • McDonough, P.M., Hanford, D.S., Sprenkle, A.B., Mellon, N.R., and Glembotski, C.C. (1997). Collaborative roles for c-Jun N-terminal kinase, c-Jun, serum response factor, and Sp1 in calcium-regulated myocardial gene expression. J. Biol. Chem. 272, 24046-24053.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24046-24053
    • McDonough, P.M.1    Hanford, D.S.2    Sprenkle, A.B.3    Mellon, N.R.4    Glembotski, C.C.5
  • 31
    • 0033537842 scopus 로고    scopus 로고
    • A post-transcriptional compensatory pathway in heterozygous ventricular myosin light chain 2-deficient mice results in lack of gene dosage effect during normal cardiac growth or hypertrophy
    • Minamisawa, S., Gu, Y., Ross, J., Jr., Chien, K.R., and Chen, J. (1999). A post-transcriptional compensatory pathway in heterozygous ventricular myosin light chain 2-deficient mice results in lack of gene dosage effect during normal cardiac growth or hypertrophy. J. Biol. Chem. 274, 10066-10070.
    • (1999) J. Biol. Chem. , vol.274 , pp. 10066-10070
    • Minamisawa, S.1    Gu, Y.2    Ross Jr., J.3    Chien, K.R.4    Chen, J.5
  • 33
    • 0025773177 scopus 로고
    • Abnormal intracellular modulation of calcium as a major cause of cardiac contractile dysfunction
    • Morgan, J.P. (1991). Abnormal intracellular modulation of calcium as a major cause of cardiac contractile dysfunction. N. Engl. J. Med. 325, 625-632.
    • (1991) N. Engl. J. Med. , vol.325 , pp. 625-632
    • Morgan, J.P.1
  • 34
    • 0032076955 scopus 로고    scopus 로고
    • Actin mutations in dilated cardiomyopathy, a heritable form of heart failure
    • Olson, T.M., Michels, V.V., Thibodeau, S.N., Tai, Y.S., and Keating, M.T. (1998). Actin mutations in dilated cardiomyopathy, a heritable form of heart failure. Science 280, 750-752.
    • (1998) Science , vol.280 , pp. 750-752
    • Olson, T.M.1    Michels, V.V.2    Thibodeau, S.N.3    Tai, Y.S.4    Keating, M.T.5
  • 35
    • 0030833435 scopus 로고    scopus 로고
    • Force-frequency effect is a powerful determinant of myocardial contractility in the mouse
    • Palakodeti, V., Oh, S., Oh, B.H., Mao, L., Hongo, M., Peterson, K.L., and Ross, J., Jr. (1997). Force-frequency effect is a powerful determinant of myocardial contractility in the mouse. Am. J. Physiol. 273, H1283-H1290.
    • (1997) Am. J. Physiol. , vol.273
    • Palakodeti, V.1    Oh, S.2    Oh, B.H.3    Mao, L.4    Hongo, M.5    Peterson, K.L.6    Ross Jr., J.7
  • 37
    • 33747550459 scopus 로고    scopus 로고
    • Downregulation of sarcoplasmic reticulum Ca(2+)-ATPase during progression of left ventricular hypertrophy
    • Qi, M., Shannon, T.R., Euler, D.E., Bers, D.M., and Samarel, A.M. (1997). Downregulation of sarcoplasmic reticulum Ca(2+)-ATPase during progression of left ventricular hypertrophy. Am. J. Physiol. 272, H2416-H2424.
    • (1997) Am. J. Physiol. , vol.272
    • Qi, M.1    Shannon, T.R.2    Euler, D.E.3    Bers, D.M.4    Samarel, A.M.5
  • 38
    • 0030609163 scopus 로고    scopus 로고
    • 2+ /calmodulin-dependent protein kinase II regulates atrial natriuretic factor gene expression in ventricular myocytes
    • 2+ /calmodulin-dependent protein kinase II regulates atrial natriuretic factor gene expression in ventricular myocytes. J. Biol. Chem. 272, 31203-31208.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31203-31208
    • Ramirez, M.T.1    Zhao, X.L.2    Schulman, H.3    Brown, J.H.4
  • 41
    • 0032561337 scopus 로고    scopus 로고
    • Cardiacspecific overexpression of mouse cardiac calsequestrin is associated with depressed cardiovascular function and hypertrophy in transgenic mice
    • Sato, Y., Ferguson, D.G., Sako, H., Dorn, G.W. II, Kadambi, V.J. , Yatani, A., Hoit, B.D., Walsh, R.A., and Kranias, E.G. (1998). Cardiacspecific overexpression of mouse cardiac calsequestrin is associated with depressed cardiovascular function and hypertrophy in transgenic mice. J. Biol. Chem. 273, 28470-28477.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28470-28477
    • Sato, Y.1    Ferguson, D.G.2    Sako, H.3    Dorn II, G.W.4    Kadambi, V.J.5    Yatani, A.6    Hoit, B.D.7    Walsh, R.A.8    Kranias, E.G.9
  • 42
    • 0032865827 scopus 로고    scopus 로고
    • Human heart failure: CAMP stimulation of SR Ca(2 + )-ATPase activity and phosphorylation level of phospholamban
    • Schmidt, U., Hajjar, R.J., Kim, C.S., Lebeche, D., Doye, A.A., and Gwathmey, U.K. (1999). Human heart failure: cAMP stimulation of SR Ca(2 + )-ATPase activity and phosphorylation level of phospholamban. Am. J. Physiol. 277, H474-H480.
    • (1999) Am. J. Physiol. , vol.277
    • Schmidt, U.1    Hajjar, R.J.2    Kim, C.S.3    Lebeche, D.4    Doye, A.A.5    Gwathmey, U.K.6
  • 43
    • 0033105384 scopus 로고    scopus 로고
    • Reduced Ca(2+)-sensitivity of SERCA 2a in failing human myocardium due to reduced serine-16 phospholamban phosphorylation
    • Schwinger, R.H., Munch, G., Bolck, B., Karczewski, P., Krause, E.G., and Erdmann, E. (1999). Reduced Ca(2+)-sensitivity of SERCA 2a in failing human myocardium due to reduced serine-16 phospholamban phosphorylation. J. Mol. Cell. Cardiol. 31, 479-491.
    • (1999) J. Mol. Cell. Cardiol. , vol.31 , pp. 479-491
    • Schwinger, R.H.1    Munch, G.2    Bolck, B.3    Karczewski, P.4    Krause, E.G.5    Erdmann, E.6
  • 44
    • 0031722958 scopus 로고    scopus 로고
    • Phospholamban: Protein structure, mechanism of action, and role in cardiac function
    • Simmerman, H.K., and Jones, L.R. (1998). Phospholamban: protein structure, mechanism of action, and role in cardiac function. Physiol. Rev. 78, 921-947.
    • (1998) Physiol. Rev. , vol.78 , pp. 921-947
    • Simmerman, H.K.1    Jones, L.R.2
  • 45
    • 0015594940 scopus 로고
    • Mitochondria and sarcoplasmic reticulum function in cardiac hypertrophy and failure
    • Sordahl, LA., McCollum, W.B., Wood, W.G., and Schwartz, A. (1973). Mitochondria and sarcoplasmic reticulum function in cardiac hypertrophy and failure. Am. J. Physiol. 224, 497-502.
    • (1973) Am. J. Physiol. , vol.224 , pp. 497-502
    • Sordahl, L.A.1    McCollum, W.B.2    Wood, W.G.3    Schwartz, A.4
  • 46
    • 0031702491 scopus 로고    scopus 로고
    • Molecular regulation of phospholamban function and expression
    • Tada, M., and Toyofuku, T. (1998). Molecular regulation of phospholamban function and expression. Trends Cardiovasc. Med. 8, 330-340.
    • (1998) Trends Cardiovasc. Med. , vol.8 , pp. 330-340
    • Tada, M.1    Toyofuku, T.2
  • 47
    • 0020489378 scopus 로고
    • Calcium transport by cardiac sarcoplasmic reticulum and phosphorylation of phospholamban
    • Tada, M., Yamada, M., Kadoma, M., Inui, M., and Ohmori, F. (1982). Calcium transport by cardiac sarcoplasmic reticulum and phosphorylation of phospholamban. Mol. Cell. Biochem. 46, 73-95.
    • (1982) Mol. Cell. Biochem. , vol.46 , pp. 73-95
    • Tada, M.1    Yamada, M.2    Kadoma, M.3    Inui, M.4    Ohmori, F.5
  • 49
    • 0028169263 scopus 로고
    • Amino acids Glu2 to Ile18 in the cytoplasmic domain of phospholamban are essential for functional association with the Ca(2+)-ATPase of sarcoplasmic reticulum
    • Toyofuku, T., Kurzydlowski, K., Tada, M., and MacLennan, D.H. (1994). Amino acids Glu2 to Ile18 in the cytoplasmic domain of phospholamban are essential for functional association with the Ca(2+)-ATPase of sarcoplasmic reticulum. J. Biol. Chem. 269,3088-3094.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3088-3094
    • Toyofuku, T.1    Kurzydlowski, K.2    Tada, M.3    MacLennan, D.H.4
  • 50
    • 0031939753 scopus 로고    scopus 로고
    • Cardiac muscle cell hypertrophy and apoptosis induced by distinct members of the p38 mitogen-activated protein kinase family
    • Wang, Y., Huang, S., Sah, V.P., Ross, J., Jr., Brown, J.H., Han, J., and Chien, K.R. (1998). Cardiac muscle cell hypertrophy and apoptosis induced by distinct members of the p38 mitogen-activated protein kinase family. J. Biol. Chem. 273, 2161-2168.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2161-2168
    • Wang, Y.1    Huang, S.2    Sah, V.P.3    Ross Jr., J.4    Brown, J.H.5    Han, J.6    Chien, K.R.7
  • 51
    • 0030957101 scopus 로고    scopus 로고
    • Ionic mechanism of the effects of hydrogen peroxide in rat ventricular myocytes
    • Ward, C.A., and Giles, W.R. (1997). Ionic mechanism of the effects of hydrogen peroxide in rat ventricular myocytes. J. Physiol. (Lond.) 500, 631-642.
    • (1997) J. Physiol. (Lond.) , vol.500 , pp. 631-642
    • Ward, C.A.1    Giles, W.R.2
  • 52
    • 0023877521 scopus 로고
    • Calcium transport properties of cardiac sarcoplasmic reticulum from cardiomyopathic Syrian hamsters (BIO 53.58 and 14.6): Evidence for a quantitative defect in dilated myopathic hearts not evident in hypertrophie hearts
    • Whitmer, J.T., Kumar, P., and Solaro, R.J. (1988). Calcium transport properties of cardiac sarcoplasmic reticulum from cardiomyopathic Syrian hamsters (BIO 53.58 and 14.6): evidence for a quantitative defect in dilated myopathic hearts not evident in hypertrophie hearts. Circ. Res. 62, 81-85.
    • (1988) Circ. Res. , vol.62 , pp. 81-85
    • Whitmer, J.T.1    Kumar, P.2    Solaro, R.J.3


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